Biofunctional peptide design
Published:12 Nov 2013
De novo peptide design provides an efficient strategy to emulate native folding elements. Polypeptide sequences are arranged into secondary structure oligomers, which can be continuous, that is belonging to one sequence, non-covalent, but monodisperse and autonomously folded, and supramolecular leading to nanostructured assemblies, which are not necessarily discrete and uniform. Despite the diversity of sequences and functions they encode there exist relatively few arrangement types, with each being associated with a specific type of function. This forms the basis for the classification of polypeptide folds, which help provide a design framework for de novo peptides. Therefore, designed sequences that deliver particular biological functions can be referred to as bio-functional motifs, and strategies that are principally focused on providing such motifs constitute bio-functional peptide design. This report highlights recent developments in the field and sets out from generic design principles of conventional backbone secondary structures, both autonomously folded and self-assembling motifs, with a progress overview in designing unconventional alternative peptide backbones.